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Protein

Oxysterol-binding protein 1

Gene

Osbp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds cholesterol and a range of oxysterols. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylate ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability (By similarity).By similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. protein domain specific binding Source: MGI

GO - Biological processi

  1. lipid transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_198151. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein 1
Gene namesi
Name:Osbp
Synonyms:Kiaa4220
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:97447. Osbp.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity
Note: When bound to oxysterols, translocates to the periphery of Golgi membranes.By similarity

GO - Cellular componenti

  1. cell junction Source: MGI
  2. cytoplasm Source: MGI
  3. Golgi apparatus Source: MGI
  4. Golgi membrane Source: UniProtKB-SubCell
  5. nucleolus Source: MGI
  6. nucleoplasm Source: MGI
  7. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 805805Oxysterol-binding protein 1PRO_0000349262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphoserine3 Publications
Modified residuei191 – 1911Phosphoserine3 Publications
Modified residuei196 – 1961Phosphoserine1 Publication
Modified residuei238 – 2381Phosphoserine1 Publication
Modified residuei349 – 3491Phosphoserine3 Publications
Modified residuei375 – 3751PhosphothreonineBy similarity
Modified residuei380 – 3801Phosphoserine1 Publication
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei387 – 3871PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3B7Z2.
PaxDbiQ3B7Z2.
PRIDEiQ3B7Z2.

PTM databases

PhosphoSiteiQ3B7Z2.

Expressioni

Gene expression databases

GenevestigatoriQ3B7Z2.

Interactioni

Subunit structurei

Homodimer or homotrimer. Interacts with VAPA (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ3B7Z2.
SMRiQ3B7Z2. Positions 89-178, 344-378, 403-798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 17994PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni404 – 45552Sterol bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili289 – 32436Sequence AnalysisAdd
BLAST
Coiled coili728 – 75932Sequence AnalysisAdd
BLAST

Domaini

The PH domain control cholesterol binding without affecting 25-hydroxycholesterol binding.By similarity
The second coiled-coil domain is required for interaction with the tyrosine phosphatase.By similarity

Sequence similaritiesi

Belongs to the OSBP family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG281324.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231233.
HOVERGENiHBG053374.
InParanoidiQ3B7Z2.
OMAiVGSGKDQ.
OrthoDBiEOG7MPRD7.
TreeFamiTF320922.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3B7Z2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAATELRGVV GPGPAAIAAP GGGGAGPPAV GGGGGRGDAG PGPGVAAATA
60 70 80 90 100
ATAGGPGPGA GGVAAGGPGS APPAAGSGGS GAGGSGSARE GWLFKWTNYI
110 120 130 140 150
KGYQRRWFVL SNGLLSYYRS KAEMRHTCRG TINLATANIT VEDSCNFIIS
160 170 180 190 200
NGGAQTYHLK ASSEVERQRW VTALELAKAK AVKMLAESDD SGDEESVSQT
210 220 230 240 250
DKTELQSTLR TLSSKVEDLS TCNDLIAKHG TALQRSLSEL ESLKLPAESN
260 270 280 290 300
EKIKQVNERA TLFRITSNAM INACRDFLML AQTHSKKWQK SLQYERDQRI
310 320 330 340 350
RLEETLEQLA KQHNHLERAF RGATVLPANP PGSAGSGKDQ CCSGKGDMSD
360 370 380 390 400
EDDENEFFDA PEIITMPENL GHKRTGSNIS GASSDVSLDE QYKHQLEETK
410 420 430 440 450
KEKRTRIPYK PNYSLNLWSI MKNCIGKELS KIPMPVNFNE PLSMLQRLTE
460 470 480 490 500
DLEYHELLDR AAKCENSLEQ LCYVAAFTVS SYSTTVFRTS KPFNPLLGET
510 520 530 540 550
FELDRLEENG YRSICEQVSH HPPAAAHHAE SKNGWTLRQE IKITSKFRGK
560 570 580 590 600
YLSIMPLGTI HCIFHSTGHH YTWKKVTTTV HNIIVGKLWI DQSGEIDIVN
610 620 630 640 650
HKTGDKCNLK FVPYSYFSRD VARKVTGEVT DPSGKVHFAL LGTWDEKMDC
660 670 680 690 700
FKVQAASGEN GGDARQRGHE AEDSRVMLWK RNPLPKNAEN MYYFSELALT
710 720 730 740 750
LNAWEGGTAP TDSRLRPDQR LMENGRWDEA NAEKQRLEEK QRLSRKKREA
760 770 780 790 800
EAAKATEDGT PHDPYKALWF ERKKDPVTRE LTHIYSGEYW ECKEKQDWGS

CPDIF
Length:805
Mass (Da):88,797
Last modified:February 6, 2013 - v3
Checksum:i0922E5C6D660B425
GO
Isoform 2 (identifier: Q3B7Z2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-268: Missing.
     269-272: AMIN → MLQL

Note: No experimental confirmation available.

Show »
Length:537
Mass (Da):61,670
Checksum:i6FF692745FD305DC
GO

Sequence cautioni

The sequence AAI07328.1 differs from that shown.Probable cloning artifact.Curated
The sequence AAI07329.1 differs from that shown.Probable cloning artifact.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 268268Missing in isoform 2. 1 PublicationVSP_035281Add
BLAST
Alternative sequencei269 – 2724AMIN → MLQL in isoform 2. 1 PublicationVSP_035282

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132663 mRNA. Translation: BAE21289.1.
AC124464 Genomic DNA. No translation available.
BC094342 mRNA. Translation: AAH94342.1.
BC107327 mRNA. Translation: AAI07328.1. Sequence problems.
BC107328 mRNA. Translation: AAI07329.1. Sequence problems.
AK220301 mRNA. Translation: BAD90226.1.
CCDSiCCDS37925.1. [Q3B7Z2-1]
RefSeqiNP_001028346.1. NM_001033174.1. [Q3B7Z2-1]
XP_006527502.1. XM_006527439.1. [Q3B7Z2-2]
UniGeneiMm.291279.

Genome annotation databases

EnsembliENSMUST00000025590; ENSMUSP00000025590; ENSMUSG00000024687. [Q3B7Z2-1]
GeneIDi76303.
KEGGimmu:76303.
UCSCiuc008gtk.1. mouse. [Q3B7Z2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132663 mRNA. Translation: BAE21289.1.
AC124464 Genomic DNA. No translation available.
BC094342 mRNA. Translation: AAH94342.1.
BC107327 mRNA. Translation: AAI07328.1. Sequence problems.
BC107328 mRNA. Translation: AAI07329.1. Sequence problems.
AK220301 mRNA. Translation: BAD90226.1.
CCDSiCCDS37925.1. [Q3B7Z2-1]
RefSeqiNP_001028346.1. NM_001033174.1. [Q3B7Z2-1]
XP_006527502.1. XM_006527439.1. [Q3B7Z2-2]
UniGeneiMm.291279.

3D structure databases

ProteinModelPortaliQ3B7Z2.
SMRiQ3B7Z2. Positions 89-178, 344-378, 403-798.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ3B7Z2.

Proteomic databases

MaxQBiQ3B7Z2.
PaxDbiQ3B7Z2.
PRIDEiQ3B7Z2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025590; ENSMUSP00000025590; ENSMUSG00000024687. [Q3B7Z2-1]
GeneIDi76303.
KEGGimmu:76303.
UCSCiuc008gtk.1. mouse. [Q3B7Z2-2]

Organism-specific databases

CTDi5007.
MGIiMGI:97447. Osbp.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG281324.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231233.
HOVERGENiHBG053374.
InParanoidiQ3B7Z2.
OMAiVGSGKDQ.
OrthoDBiEOG7MPRD7.
TreeFamiTF320922.

Enzyme and pathway databases

ReactomeiREACT_198151. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiOsbp. mouse.
NextBioi344933.
PROiQ3B7Z2.
SOURCEiSearch...

Gene expression databases

GenevestigatoriQ3B7Z2.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-805.
    Strain: C57BL/6.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-805.
    Tissue: Pancreatic islet.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-196; SER-349 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-238 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiOSBP1_MOUSE
AccessioniPrimary (citable) accession number: Q3B7Z2
Secondary accession number(s): E9QPD4
, Q3V163, Q52KH7, Q570Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 6, 2013
Last modified: March 4, 2015
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.